Karsisiotis, Andreas Ioannis and Deacon, Oliver M and Macdonald, Colin and Blumenschein, Tharin MA and Moore, Geoffrey R and Worrall, Jonathan AR (2017) 'Near-complete backbone resonance assignments of acid-denatured human cytochrome c in dimethylsulfoxide: a prelude to studying interactions with phospholipids.' Biomolecular NMR Assignments, 11 (2). pp. 165-168. ISSN 1874-2718
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Abstract
Human cytochrome c plays a central role in the mitochondrial electron transfer chain and in the intrinsic apoptosis pathway. Through the interaction with the phospholipid cardiolipin, cytochrome c triggers release of pro-apoptotic factors, including itself, from the mitochondrion into the cytosol of cells undergoing apoptosis. The cytochrome c/cardiolipin complex has been extensively studied through various spectroscopies, most recently with high-field solution and solid-state NMR spectroscopies, but there is no agreement between the various studies on key structural features of cytochrome c in its complex with cardiolipin. In the present study, we report backbone 1H, 13C, 15N resonance assignments of acid-denatured human cytochrome c in the aprotic solvent dimethylsulfoxide. These have led to the assignment of a reference 2D 1H-15N HSQC spectrum in which out of the 99 non-proline residues 87% of the backbone amides are assigned. These assignments are being used in an interrupted H/D exchange strategy to map the binding site of cardiolipin on human cytochrome c.
Item Type: | Article |
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Uncontrolled Keywords: | Human cytochrome c; Apoptosis; Cardiolipin; Acid-denatured; DMSO |
Subjects: | Q Science > QD Chemistry |
Divisions: | Faculty of Science and Health Faculty of Science and Health > Life Sciences, School of |
SWORD Depositor: | Elements |
Depositing User: | Elements |
Date Deposited: | 19 Apr 2017 15:57 |
Last Modified: | 06 Jan 2022 14:46 |
URI: | http://repository.essex.ac.uk/id/eprint/19487 |
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